During the past year, the laboratory focused on Ebola glycoprotein structural biology studies using antibodies to form a Fab:glycoprotein complex, which will generate a more stable protein and give an increased probability of generating crystals from the conditions that are screened. There were also efforts directed to increasing the chances of crystallization by cleaving the glycoprotein with a protease enzyme that is critical for Ebola virus entry. The lab developed a procedure to cleave Ebola-GP trimer into a much smaller trimer resembling the physiological intermediate formed in the endosome of host cells. This intermediate can be used as a tool to help find the receptor for Ebola virus as well as serve as a possible immunogen.